FMO DATABASE

FMODB ID: LGL29

Calculation Name: 2WL7-A-Xray547

Preferred Name:

Target Type:

Ligand Name: chloride ion

Ligand 3-letter code: CL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2WL7

Chain ID: A

ChEMBL ID:

UniProt ID: Q91XM9

Base Structure: X-ray

Registration Date: 2025-10-04

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	96
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-658159.302968
FMO2-HF: Nuclear repulsion	622024.159829
FMO2-HF: Total energy	-36135.14314
FMO2-MP2: Total energy	-36242.252625

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:95:GLU)

Summations of interaction energy for fragment #1(A:95:GLU)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-1.182	2.377	-0.019	-1.663	-1.879	-0.002

Interaction energy analysis for fragmet #1(A:95:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.087 / q_NPA : -0.048

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	97	GLU	-1	-0.863	-0.908	3.848	-16.053	-13.670	-0.025	-1.260	-1.098	-0.002
92	A	186	ARG	1	0.970	0.974	4.141	-8.598	-8.534	-0.001	-0.042	-0.022	0.000
93	A	187	ARG	1	0.856	0.921	3.382	17.492	18.434	0.008	-0.356	-0.595	0.000
94	A	188	PRO	0	0.001	-0.008	5.040	0.614	0.784	-0.001	-0.005	-0.164	0.000
4	A	98	PHE	0	-0.005	-0.010	6.540	2.191	2.191	0.000	0.000	0.000	0.000
5	A	99	GLU	-1	-0.809	-0.894	10.057	-3.220	-3.220	0.000	0.000	0.000	0.000
6	A	100	GLU	-1	-0.904	-0.937	13.658	-0.771	-0.771	0.000	0.000	0.000	0.000
7	A	101	ILE	0	-0.023	-0.015	15.818	-0.107	-0.107	0.000	0.000	0.000	0.000
8	A	102	THR	0	-0.035	-0.041	19.461	0.269	0.269	0.000	0.000	0.000	0.000
9	A	103	LEU	0	-0.023	0.003	21.574	-0.041	-0.041	0.000	0.000	0.000	0.000
10	A	104	GLU	-1	-0.908	-0.958	24.807	-0.437	-0.437	0.000	0.000	0.000	0.000
11	A	105	ARG	1	0.752	0.858	27.633	-0.079	-0.079	0.000	0.000	0.000	0.000
12	A	106	GLY	0	0.038	0.014	29.440	0.013	0.013	0.000	0.000	0.000	0.000
13	A	107	ASN	0	-0.012	-0.027	32.952	0.048	0.048	0.000	0.000	0.000	0.000
14	A	108	SER	0	-0.014	0.006	30.995	0.040	0.040	0.000	0.000	0.000	0.000
15	A	109	GLY	0	-0.007	0.014	29.834	0.045	0.045	0.000	0.000	0.000	0.000
16	A	110	LEU	0	0.021	-0.006	23.909	-0.050	-0.050	0.000	0.000	0.000	0.000
17	A	111	GLY	0	0.034	0.031	24.708	-0.063	-0.063	0.000	0.000	0.000	0.000
18	A	112	PHE	0	-0.002	-0.003	20.493	-0.063	-0.063	0.000	0.000	0.000	0.000
19	A	113	SER	0	-0.046	-0.016	21.503	0.015	0.015	0.000	0.000	0.000	0.000
20	A	114	ILE	0	0.026	0.011	18.417	-0.023	-0.023	0.000	0.000	0.000	0.000
21	A	115	ALA	0	-0.014	-0.010	17.645	-0.085	-0.085	0.000	0.000	0.000	0.000
22	A	116	GLY	0	0.031	0.034	16.089	0.148	0.148	0.000	0.000	0.000	0.000
23	A	117	GLY	0	0.061	0.027	16.501	-0.424	-0.424	0.000	0.000	0.000	0.000
24	A	118	THR	0	-0.012	-0.037	17.789	0.149	0.149	0.000	0.000	0.000	0.000
25	A	119	ASP	-1	-0.910	-0.944	18.857	1.786	1.786	0.000	0.000	0.000	0.000
26	A	120	ASN	0	-0.060	-0.034	19.836	0.023	0.023	0.000	0.000	0.000	0.000
27	A	121	PRO	0	0.045	0.035	14.463	-0.078	-0.078	0.000	0.000	0.000	0.000
28	A	122	HIS	0	0.003	0.009	13.730	-0.189	-0.189	0.000	0.000	0.000	0.000
29	A	123	ILE	0	-0.060	-0.039	9.121	-0.009	-0.009	0.000	0.000	0.000	0.000
30	A	124	GLY	0	-0.023	-0.005	10.986	1.012	1.012	0.000	0.000	0.000	0.000
31	A	125	ASP	-1	-0.872	-0.938	11.975	4.238	4.238	0.000	0.000	0.000	0.000
32	A	126	ASP	-1	-0.851	-0.917	8.455	8.274	8.274	0.000	0.000	0.000	0.000
33	A	127	PRO	0	0.000	-0.003	11.207	-0.663	-0.663	0.000	0.000	0.000	0.000
34	A	128	GLY	0	0.024	0.010	12.308	-0.617	-0.617	0.000	0.000	0.000	0.000
35	A	129	ILE	0	-0.007	-0.004	13.296	-0.126	-0.126	0.000	0.000	0.000	0.000
36	A	130	PHE	0	-0.008	-0.006	9.140	-0.356	-0.356	0.000	0.000	0.000	0.000
37	A	131	ILE	0	0.000	0.008	14.331	-0.154	-0.154	0.000	0.000	0.000	0.000
38	A	132	THR	0	0.004	-0.007	15.735	-0.008	-0.008	0.000	0.000	0.000	0.000
39	A	133	LYS	1	0.879	0.928	18.260	-0.644	-0.644	0.000	0.000	0.000	0.000
40	A	134	ILE	0	0.048	0.031	18.089	0.030	0.030	0.000	0.000	0.000	0.000
41	A	135	ILE	0	-0.049	-0.024	22.121	0.018	0.018	0.000	0.000	0.000	0.000
42	A	136	PRO	0	0.022	-0.005	25.951	-0.054	-0.054	0.000	0.000	0.000	0.000
43	A	137	GLY	0	0.041	0.040	28.096	0.060	0.060	0.000	0.000	0.000	0.000
44	A	138	GLY	0	-0.011	-0.014	27.718	0.022	0.022	0.000	0.000	0.000	0.000
45	A	139	ALA	0	0.012	0.000	26.197	-0.058	-0.058	0.000	0.000	0.000	0.000
46	A	140	ALA	0	0.008	-0.008	21.256	-0.093	-0.093	0.000	0.000	0.000	0.000
47	A	141	ALA	0	-0.069	-0.025	22.448	-0.114	-0.114	0.000	0.000	0.000	0.000
48	A	142	GLU	-1	-0.917	-0.964	24.551	-0.547	-0.547	0.000	0.000	0.000	0.000
49	A	143	ASP	-1	-0.826	-0.878	21.525	-1.198	-1.198	0.000	0.000	0.000	0.000
50	A	144	GLY	0	0.022	0.019	21.839	-0.141	-0.141	0.000	0.000	0.000	0.000
51	A	145	ARG	1	0.786	0.885	17.722	1.227	1.227	0.000	0.000	0.000	0.000
52	A	146	LEU	0	-0.006	0.006	15.834	-0.189	-0.189	0.000	0.000	0.000	0.000
53	A	147	ARG	1	0.835	0.898	13.676	1.925	1.925	0.000	0.000	0.000	0.000
54	A	148	VAL	0	0.006	-0.004	14.878	0.243	0.243	0.000	0.000	0.000	0.000
55	A	149	ASN	0	-0.081	-0.054	10.718	0.214	0.214	0.000	0.000	0.000	0.000
56	A	150	ASP	-1	-0.747	-0.829	10.352	-1.028	-1.028	0.000	0.000	0.000	0.000
57	A	151	CYS	0	-0.052	-0.019	9.813	0.352	0.352	0.000	0.000	0.000	0.000
58	A	152	ILE	0	-0.004	-0.008	11.689	-0.555	-0.555	0.000	0.000	0.000	0.000
59	A	153	LEU	0	0.012	0.006	10.222	0.382	0.382	0.000	0.000	0.000	0.000
60	A	154	ARG	1	0.877	0.944	14.589	0.061	0.061	0.000	0.000	0.000	0.000
61	A	155	VAL	0	0.024	0.014	18.064	-0.171	-0.171	0.000	0.000	0.000	0.000
62	A	156	ASN	0	0.004	-0.001	21.224	0.001	0.001	0.000	0.000	0.000	0.000
63	A	157	GLU	-1	-0.957	-0.977	22.377	-0.134	-0.134	0.000	0.000	0.000	0.000
64	A	158	VAL	0	-0.007	-0.003	22.527	0.053	0.053	0.000	0.000	0.000	0.000
65	A	159	ASP	-1	-0.854	-0.909	17.496	1.350	1.350	0.000	0.000	0.000	0.000
66	A	160	VAL	0	-0.045	-0.040	16.858	0.008	0.008	0.000	0.000	0.000	0.000
67	A	161	SER	0	-0.025	-0.041	13.890	0.225	0.225	0.000	0.000	0.000	0.000
68	A	162	GLU	-1	-0.955	-0.976	14.694	3.774	3.774	0.000	0.000	0.000	0.000
69	A	163	VAL	0	-0.035	0.002	17.236	-0.294	-0.294	0.000	0.000	0.000	0.000
70	A	164	SER	0	0.031	0.026	19.429	0.154	0.154	0.000	0.000	0.000	0.000
71	A	165	HIS	0	-0.015	-0.027	20.358	-0.290	-0.290	0.000	0.000	0.000	0.000
72	A	166	SER	0	-0.048	-0.022	22.222	-0.163	-0.163	0.000	0.000	0.000	0.000
73	A	167	LYS	1	0.844	0.890	23.724	-0.914	-0.914	0.000	0.000	0.000	0.000
74	A	168	ALA	0	0.041	0.036	20.505	-0.106	-0.106	0.000	0.000	0.000	0.000
75	A	169	VAL	0	-0.018	-0.013	22.284	-0.158	-0.158	0.000	0.000	0.000	0.000
76	A	170	GLU	-1	-0.833	-0.888	25.196	0.599	0.599	0.000	0.000	0.000	0.000
77	A	171	ALA	0	0.056	0.025	23.135	-0.102	-0.102	0.000	0.000	0.000	0.000
78	A	172	LEU	0	0.001	-0.003	20.874	-0.134	-0.134	0.000	0.000	0.000	0.000
79	A	173	LYS	1	0.908	0.968	24.884	-0.500	-0.500	0.000	0.000	0.000	0.000
80	A	174	GLU	-1	-0.945	-0.990	28.479	0.352	0.352	0.000	0.000	0.000	0.000
81	A	175	ALA	0	-0.034	0.001	25.734	-0.051	-0.051	0.000	0.000	0.000	0.000
82	A	176	GLY	0	0.030	0.025	27.823	-0.073	-0.073	0.000	0.000	0.000	0.000
83	A	177	SER	0	-0.006	-0.020	29.603	0.013	0.013	0.000	0.000	0.000	0.000
84	A	178	ILE	0	0.012	0.022	27.515	-0.035	-0.035	0.000	0.000	0.000	0.000
85	A	179	VAL	0	0.001	0.000	22.916	0.059	0.059	0.000	0.000	0.000	0.000
86	A	180	ARG	1	0.985	1.002	18.267	0.849	0.849	0.000	0.000	0.000	0.000
87	A	181	LEU	0	0.017	0.011	17.786	0.160	0.160	0.000	0.000	0.000	0.000
88	A	182	TYR	0	-0.058	-0.027	12.059	-0.476	-0.476	0.000	0.000	0.000	0.000
89	A	183	VAL	0	0.040	0.014	12.679	0.496	0.496	0.000	0.000	0.000	0.000
90	A	184	ARG	1	0.890	0.940	6.075	-7.395	-7.395	0.000	0.000	0.000	0.000
91	A	185	ARG	1	0.751	0.838	7.701	4.784	4.784	0.000	0.000	0.000	0.000
95	A	189	ILE	0	-0.034	-0.012	5.621	-2.784	-2.784	0.000	0.000	0.000	0.000
96	A	190	LEU	-1	-0.935	-0.954	8.024	-4.335	-4.335	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:95:GLU)